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JG24_06105 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_06105" - 2-oxoglutarate dehydrogenase E1 component in Klebsiella pneumoniae
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
JG24_061052-oxoglutarate dehydrogenase E1 component; Derived by automated computational analysis using gene prediction method- Protein Homology (935 aa)    
Predicted Functional Partners:
JG24_06110
Component of 2-oxoglutarate dehydrogenase complex; catalyzes the transfer of succinyl coenzyme A to form succinyl CoA as part of the conversion of 2-oxoglutarate to succinyl-CoA; Derived by automated computational analysis using gene prediction method- Protein Homology (408 aa)
  0.999
sucD
Succinate--CoA ligase [ADP-forming] subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (289 aa)
 
 
  0.998
sucC
Succinate--CoA ligase [ADP-forming] subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (388 aa)
 
 
  0.990
JG24_08465
Isocitrate dehydrogenase [NADP]; Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method- Protein Homology (416 aa)
     
 
  0.971
JG24_03490
E3 component of alpha keto acid dehydrogenase complexes LpdC; forms a homodimer; binds one molecule of FAD monomer; catalyzes NAD+-dependent oxidation of dihydrolipoyl cofactors that are covalently linked to the E2 component; Derived by automated computational analysis using gene prediction method- Protein Homology (465 aa)
 
  0.969
JG24_30035
Dihydrolipoyl dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenase complex; catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method- Protein Homology (474 aa)
 
  0.962
sdhC
Succinate dehydrogenase cytochrome b-556 subunit; Derived by automated computational analysis using gene prediction method- Protein Homology (134 aa)
 
   
  0.954
gltB
Glutamate synthase [NADPH] large chain; Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method- Protein Homology (1486 aa)
     
 
  0.945
sdhD
Succinate dehydrogenase hydrophobic membrane anchor subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH) (115 aa)
   
   
  0.932
JG24_06080
Citrate synthase; Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the citrate [...] (427 aa)
 
   
  0.898
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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